Q10132 · IDI1_SCHPO
- ProteinIsopentenyl-diphosphate delta-isomerase
- Geneidi1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids229 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:7744766).
Idi1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (PubMed:7744766).
The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable)
Idi1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (PubMed:7744766).
The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable)
Catalytic activity
- isopentenyl diphosphate = dimethylallyl diphosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | substrate | ||||
Sequence: K | ||||||
Binding site | 43 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 54 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 72 | substrate | ||||
Sequence: Q | ||||||
Binding site | 77 | substrate | ||||
Sequence: K | ||||||
Active site | 89 | |||||
Sequence: C | ||||||
Binding site | 90 | substrate | ||||
Sequence: S | ||||||
Binding site | 152 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 154 | |||||
Sequence: E | ||||||
Binding site | 154 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | isopentenyl-diphosphate delta-isomerase activity | |
Molecular Function | metal ion binding | |
Biological Process | dimethylallyl diphosphate biosynthetic process | |
Biological Process | farnesyl diphosphate biosynthetic process | |
Biological Process | isopentenyl diphosphate biosynthetic process | |
Biological Process | sterol biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsopentenyl-diphosphate delta-isomerase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionQ10132
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000205230 | 1-229 | Isopentenyl-diphosphate delta-isomerase | |||
Sequence: MIMSSQQEKKDYDEEQLRLMEEVCIVVDENDVPLRYGTKKECHLMENINKGLLHRAFSMFIFDEQNRLLLQQRAEEKITFPSLWTNTCCSHPLDVAGERGNTLPEAVEGVKNAAQRKLFHELGIQAKYIPKDKFQFLTRIHYLAPSTGAWGEHEIDYILFFKGKVELDINPNEVQAYKYVTMEELKEMFSDPQYGFTPWFKLICEHFMFKWWQDVDHASKFQDTLIHRC |
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 52-202 | Nudix hydrolase | ||||
Sequence: LLHRAFSMFIFDEQNRLLLQQRAEEKITFPSLWTNTCCSHPLDVAGERGNTLPEAVEGVKNAAQRKLFHELGIQAKYIPKDKFQFLTRIHYLAPSTGAWGEHEIDYILFFKGKVELDINPNEVQAYKYVTMEELKEMFSDPQYGFTPWFKL |
Sequence similarities
Belongs to the IPP isomerase type 1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length229
- Mass (Da)27,108
- Last updated2012-07-11 v2
- ChecksumA3FE0B29B12AD9A0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329671 EMBL· GenBank· DDBJ | CAB53731.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
U21154 EMBL· GenBank· DDBJ | AAA80596.1 EMBL· GenBank· DDBJ | mRNA |